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  2. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    In computational biology, protein pK a calculations are used to estimate the pK a values of amino acids as they exist within proteins.These calculations complement the pK a values reported for amino acids in their free state, and are used frequently within the fields of molecular modeling, structural bioinformatics, and computational biology.

  3. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Also, amino acid side chain affinity for water was measured using vapor phases. [14] Vapor phases represent the simplest non polar phases, because it has no interaction with the solute. [ 18 ] The hydration potential and its correlation to the appearance of amino acids on the surface of proteins was studied by Wolfenden.

  4. Acid dissociation constant - Wikipedia

    en.wikipedia.org/wiki/Acid_dissociation_constant

    The hydroxide ion OH −, a well known base, is here acting as the conjugate base of the acid water. Acids and bases are thus regarded simply as donors and acceptors of protons respectively. A broader definition of acid dissociation includes hydrolysis, in which protons are produced by the splitting of water molecules.

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The polar, uncharged amino acids serine (Ser, S), threonine (Thr, T), asparagine (Asn, N) and glutamine (Gln, Q) readily form hydrogen bonds with water and other amino acids. [32] They do not ionize in normal conditions, a prominent exception being the catalytic serine in serine proteases. This is an example of severe perturbation, and is not ...

  6. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    The N-O distance required is less than 4 Å (400 pm). Amino acids greater than this distance apart do not qualify as forming a salt bridge. [11] Due to the numerous ionizable side chains of amino acids found throughout a protein, the pH at which a protein is placed is crucial to its stability.

  7. Molecular Operating Environment - Wikipedia

    en.wikipedia.org/wiki/Molecular_Operating...

    AlphaFold is the most advanced system to date that can accurately predict a protein's 3D structure from its amino acid sequence. [30] The protein folding problem first began to emerge around the 1960s and ever since, scientists have struggled in determining methods to precisely predict the way a protein will fold solely based on the amino acid ...

  8. Bovine serum albumin - Wikipedia

    en.wikipedia.org/wiki/Bovine_serum_albumin

    Bovine serum albumin (BSA or "Fraction V") is a serum albumin protein derived from cows. It is often used as a protein concentration standard in lab experiments. The nickname "Fraction V" refers to albumin being the fifth fraction of the original Edwin Cohn purification methodology that made use of differential solubility characteristics of plasma proteins.

  9. Acid strength - Wikipedia

    en.wikipedia.org/wiki/Acid_strength

    Acetic acid is said to be a differentiating solvent for the three acids, while water is not. [6]: (p. 217) An important example of a solvent which is more basic than water is dimethyl sulfoxide, DMSO, (). A compound which is a weak acid in water may become a strong acid in DMSO.